Literature summary for 1.17.4.1 extracted from

Chen, X.; Xu, Z.; Zhang, L.; Liu, H.; Liu, X.; Lou, M.; Zhu, L.; Huang, B.; Yang, C.G.; Zhu, W.; Shao, J.
The conserved Lys-95 charged residue cluster is critical for the homodimerization and enzyme activity of human ribonucleotide reductase small subunit m2 (2014), J. Biol. Chem., 289, 909-920.

Search for more literature for 1.17.4.1

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
K95E	mutation in small subunit M2, results in dimer disassembly and enzyme activity inhibition. Mutant is capable of generating the diiron and tyrosyl radical cofactor, but the disassembly of the M2 dimer reduces its interaction with the large subunit M1. The transfection of the wild-type M2 but not the K95E mutant rescues theG1/S phase cell cycle arrest and cell growth inhibition caused by the siRNA knockdown of M2	Homo sapiens
K95E/E98K	charge-exchanging double mutation, recovers the dimerization and activity lost in mutant K95E	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P31350	small subunit RIR2	-

Synonyms

Synonyms	Comment	Organism
RIR2	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	a conserved cluster of charged residues, including Lys95, Glu98, Glu-05, and Glu174, at the interface may function as an ionic lock for small subunit M2 homodimer. The transfection of the wild-type small subunit M2 but not the K95E mutant rescues theG1/S phase cell cycle arrest and cell growth inhibition caused by the siRNA knockdown of M2	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)